ID KGUA_DECAR Reviewed; 202 AA. AC Q479A8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328}; DE EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328}; DE AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328}; GN Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; GN OrderedLocusNames=Daro_3845; OS Dechloromonas aromatica (strain RCB). OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae; OC Dechloromonas. OX NCBI_TaxID=159087; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCB; RX PubMed=19650930; DOI=10.1186/1471-2164-10-351; RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., RA Lapidus A.; RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: RT indications of a surprisingly complex life-style and cryptic anaerobic RT pathways for aromatic degradation."; RL BMC Genomics 10:351-351(2009). CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:456216; EC=2.7.4.8; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00328}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000255|HAMAP- CC Rule:MF_00328}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000089; AAZ48573.1; -; Genomic_DNA. DR AlphaFoldDB; Q479A8; -. DR SMR; Q479A8; -. DR STRING; 159087.Daro_3845; -. DR KEGG; dar:Daro_3845; -. DR eggNOG; COG0194; Bacteria. DR HOGENOM; CLU_001715_1_2_4; -. DR OrthoDB; 9808150at2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004385; F:guanylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00071; GMPK; 1. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00328; Guanylate_kinase; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR017665; Guanylate_kinase. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR03263; guanyl_kin; 1. DR PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1. DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR SMART; SM00072; GuKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1..202 FT /note="Guanylate kinase" FT /id="PRO_0000266313" FT DOMAIN 3..181 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" FT BINDING 10..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00328" SQ SEQUENCE 202 AA; 22582 MW; A39C84F5D61CE951 CRC64; MAGNLFVVAA PSGAGKTTLV RMLLEQESSV NLSISYTTRH PRPGEQNGRE YHFVETPEFR AMIARQEFLE WAEVHGNFYG TSKKWIADQL AAGRDVLLEI DWQGAQQVRA LFPQAIGVFI LPPSMEELTR RLTGRGTDSP DVIDRRLAAA QAEMRHVGEF DYVIINDQLA QALDDLRAVV RASGLSFGAQ RARHAALFER MI //